Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
fliPFlagellar biosynthetic protein flip; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (245 aa)    
Predicted Functional Partners:
fliF
Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
 
 0.999
flhB
Flagellar biosynthesis protein FlhB; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family.
 
 
 0.999
flgC
With FlgF and B makes up the proximal portion of the flagellar basal body rod; Bradyrhizobium have one thick flagellum and several thin flagella; the protein in this cluster is associated with the thin flagella; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.999
flgI
Flagellar P-ring protein FlgI; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
 
 0.999
flgH
Flagellar L-ring protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
 
 0.999
fliQ
FliQ, with proteins FliP and FliR, forms the core of the central channel in the flagella export apparatus; Bradyrhizobium have one thick flagellum and several thin flagella; the protein in this cluster is associated with the thick flagellum; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.999
fliR
Flagellar biosynthesis protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family.
 
 
 0.999
fliG
Flagellar motor switch protein FliG; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.998
fliN
Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
 
 
 0.998
fliE
Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.998
Your Current Organism:
Sinorhizobium meliloti
NCBI taxonomy Id: 382
Other names: ATCC 9930, CCUG 27879, CFBP 5561, DSM 30135, Ensifer meliloti, Ensifer sp. AC50a, Ensifer sp. AC50e, HAMBI 2148, IAM 12611, ICMP 12623, IFO 14782, JCM 20682, LMG 6133, LMG:6133, NBRC 14782, NCAIM B.01520, NRRL L-45, NZP 4027, Rhizobium meliloti, Rhizobium meliloti (megaplasmid pRME41B SYM), Rhizobium meliloti (plasmid pRmeGR4b), Rhizobium meliloti plasmid pRmeGR4b, Rhizobium sp. AC50e, S. meliloti
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